Primary structure of a zinc protease from Bacillus mesentericus strain 76.
The amino acid sequence of the neutral zinc protease from Bacillus mesentericus strain 76 (MCP 76) has been determined by using peptides derived from digests with trypsin, chymotrypsin, and cyanogen bromide and from cleavage with o-iodosobenzoic acid. The peptides were purified by means of gel filtration and reversed-phase high-performance liquid chromatography and analyzed by automatic sequencing. The protein contains 300 amino acid residues. It proved to be identical with the neutral protease deduced from the DNA precursor sequence of Bacillus subtilis. The residues for zinc and substrate binding are conserved, whereas the number of calcium binding sites is reduced compared to thermolysin. A classification of the neutral zinc protease is discussed.
Stoeva
S
S
Max-Planck-Institut für Biochemie, Abteilung Proteinchemie, Martinsried bei Muenchen, West Germany.
Kleinschmidt
T
T
Mesrob
B
B
Braunitzer
G
G
D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology*; D002268:Carboxypeptidases; D043422:Carboxypeptidases A; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin; D007463:Iodobenzoates; D008666:Metalloendopeptidases; D008969:Molecular Sequence Data; D010446:Peptide Fragments; D014357:Trypsin
D007463:Iodobenzoates; D010446:Peptide Fragments; C008154:2-iodosobenzoic acid; D002268:Carboxypeptidases; D043422:Carboxypeptidases A; D002918:Chymotrypsin; D014357:Trypsin; D008666:Metalloendopeptidases; C044194:microbial metalloproteinases